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93
Dojindo Labs sulfobiotics protein redox state monitoring kit plus
Cysteine oxidation of Prx6 is upregulated in the brains of patients with Alzheimer’s disease. Brain (hippocampus) homogenates from control subjects and patients with Alzheimer’s were investigated for cysteine oxidation of Prx6 using - <t>SulfoBiotics</t> - Protein Redox State Monitoring Kit Plus. A free protein thiol group was labeled with the Protein-SHifter Plus that contains maleimide with a high affinity toward reduced sulfhydryl groups. Each Protein-SHifter causes a 15 kDa shift. After electrophoresis, the Protein-SHifter Plus moiety was eliminated by exposure of the gel to ultraviolet light that increases the efficiency of Western blotting and allows for detection of specific proteins in biological samples. In the case of human Prx6, the protein with fully oxidized cysteine residues migrates at 25 kDa. The protein with one reduced cysteine binds to a Protein-SHifter and migrates at 40 kDa, and the protein with two reduced cysteine residues migrates at 55 kDa. Our previous study determined that the 40 kDa band depicts Prx6, in which the catalytic cysteine (Cys47) is oxidized . ( A ) Representative Western blotting results using the Prx6 antibody showing 25 kDa (0 reduced sulfhydryl), 40 kDa (1 reduced sulfhydryl), and 55 kDa (2 reduced sulfhydryl) bands. ( B ) The bar graph represents means ± SEM of the ratio of the 40 kDa Prx6 band to 55 kDa Prx6 band (N = 13 for Alzheimer’s and 5 for control). The symbol * denotes that the value is significantly different from the control value at p < 0.05. ( C ) The scattered graph represents protein carbonylation vs. Prx6 thiol oxidation (N = 18). Pearson correlation coefficient R = 0.723 (positive correlation).
Sulfobiotics Protein Redox State Monitoring Kit Plus, supplied by Dojindo Labs, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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93
LGC Standards hydroxycholesterol d4
Cysteine oxidation of Prx6 is upregulated in the brains of patients with Alzheimer’s disease. Brain (hippocampus) homogenates from control subjects and patients with Alzheimer’s were investigated for cysteine oxidation of Prx6 using - <t>SulfoBiotics</t> - Protein Redox State Monitoring Kit Plus. A free protein thiol group was labeled with the Protein-SHifter Plus that contains maleimide with a high affinity toward reduced sulfhydryl groups. Each Protein-SHifter causes a 15 kDa shift. After electrophoresis, the Protein-SHifter Plus moiety was eliminated by exposure of the gel to ultraviolet light that increases the efficiency of Western blotting and allows for detection of specific proteins in biological samples. In the case of human Prx6, the protein with fully oxidized cysteine residues migrates at 25 kDa. The protein with one reduced cysteine binds to a Protein-SHifter and migrates at 40 kDa, and the protein with two reduced cysteine residues migrates at 55 kDa. Our previous study determined that the 40 kDa band depicts Prx6, in which the catalytic cysteine (Cys47) is oxidized . ( A ) Representative Western blotting results using the Prx6 antibody showing 25 kDa (0 reduced sulfhydryl), 40 kDa (1 reduced sulfhydryl), and 55 kDa (2 reduced sulfhydryl) bands. ( B ) The bar graph represents means ± SEM of the ratio of the 40 kDa Prx6 band to 55 kDa Prx6 band (N = 13 for Alzheimer’s and 5 for control). The symbol * denotes that the value is significantly different from the control value at p < 0.05. ( C ) The scattered graph represents protein carbonylation vs. Prx6 thiol oxidation (N = 18). Pearson correlation coefficient R = 0.723 (positive correlation).
Hydroxycholesterol D4, supplied by LGC Standards, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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86
Janssen data safety monitoring
Cysteine oxidation of Prx6 is upregulated in the brains of patients with Alzheimer’s disease. Brain (hippocampus) homogenates from control subjects and patients with Alzheimer’s were investigated for cysteine oxidation of Prx6 using - <t>SulfoBiotics</t> - Protein Redox State Monitoring Kit Plus. A free protein thiol group was labeled with the Protein-SHifter Plus that contains maleimide with a high affinity toward reduced sulfhydryl groups. Each Protein-SHifter causes a 15 kDa shift. After electrophoresis, the Protein-SHifter Plus moiety was eliminated by exposure of the gel to ultraviolet light that increases the efficiency of Western blotting and allows for detection of specific proteins in biological samples. In the case of human Prx6, the protein with fully oxidized cysteine residues migrates at 25 kDa. The protein with one reduced cysteine binds to a Protein-SHifter and migrates at 40 kDa, and the protein with two reduced cysteine residues migrates at 55 kDa. Our previous study determined that the 40 kDa band depicts Prx6, in which the catalytic cysteine (Cys47) is oxidized . ( A ) Representative Western blotting results using the Prx6 antibody showing 25 kDa (0 reduced sulfhydryl), 40 kDa (1 reduced sulfhydryl), and 55 kDa (2 reduced sulfhydryl) bands. ( B ) The bar graph represents means ± SEM of the ratio of the 40 kDa Prx6 band to 55 kDa Prx6 band (N = 13 for Alzheimer’s and 5 for control). The symbol * denotes that the value is significantly different from the control value at p < 0.05. ( C ) The scattered graph represents protein carbonylation vs. Prx6 thiol oxidation (N = 18). Pearson correlation coefficient R = 0.723 (positive correlation).
Data Safety Monitoring, supplied by Janssen, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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97
AutoMate Scientific Inc activity monitor software version 5
Cysteine oxidation of Prx6 is upregulated in the brains of patients with Alzheimer’s disease. Brain (hippocampus) homogenates from control subjects and patients with Alzheimer’s were investigated for cysteine oxidation of Prx6 using - <t>SulfoBiotics</t> - Protein Redox State Monitoring Kit Plus. A free protein thiol group was labeled with the Protein-SHifter Plus that contains maleimide with a high affinity toward reduced sulfhydryl groups. Each Protein-SHifter causes a 15 kDa shift. After electrophoresis, the Protein-SHifter Plus moiety was eliminated by exposure of the gel to ultraviolet light that increases the efficiency of Western blotting and allows for detection of specific proteins in biological samples. In the case of human Prx6, the protein with fully oxidized cysteine residues migrates at 25 kDa. The protein with one reduced cysteine binds to a Protein-SHifter and migrates at 40 kDa, and the protein with two reduced cysteine residues migrates at 55 kDa. Our previous study determined that the 40 kDa band depicts Prx6, in which the catalytic cysteine (Cys47) is oxidized . ( A ) Representative Western blotting results using the Prx6 antibody showing 25 kDa (0 reduced sulfhydryl), 40 kDa (1 reduced sulfhydryl), and 55 kDa (2 reduced sulfhydryl) bands. ( B ) The bar graph represents means ± SEM of the ratio of the 40 kDa Prx6 band to 55 kDa Prx6 band (N = 13 for Alzheimer’s and 5 for control). The symbol * denotes that the value is significantly different from the control value at p < 0.05. ( C ) The scattered graph represents protein carbonylation vs. Prx6 thiol oxidation (N = 18). Pearson correlation coefficient R = 0.723 (positive correlation).
Activity Monitor Software Version 5, supplied by AutoMate Scientific Inc, used in various techniques. Bioz Stars score: 97/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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93
Olympus cm20 incubation monitoring system
Cysteine oxidation of Prx6 is upregulated in the brains of patients with Alzheimer’s disease. Brain (hippocampus) homogenates from control subjects and patients with Alzheimer’s were investigated for cysteine oxidation of Prx6 using - <t>SulfoBiotics</t> - Protein Redox State Monitoring Kit Plus. A free protein thiol group was labeled with the Protein-SHifter Plus that contains maleimide with a high affinity toward reduced sulfhydryl groups. Each Protein-SHifter causes a 15 kDa shift. After electrophoresis, the Protein-SHifter Plus moiety was eliminated by exposure of the gel to ultraviolet light that increases the efficiency of Western blotting and allows for detection of specific proteins in biological samples. In the case of human Prx6, the protein with fully oxidized cysteine residues migrates at 25 kDa. The protein with one reduced cysteine binds to a Protein-SHifter and migrates at 40 kDa, and the protein with two reduced cysteine residues migrates at 55 kDa. Our previous study determined that the 40 kDa band depicts Prx6, in which the catalytic cysteine (Cys47) is oxidized . ( A ) Representative Western blotting results using the Prx6 antibody showing 25 kDa (0 reduced sulfhydryl), 40 kDa (1 reduced sulfhydryl), and 55 kDa (2 reduced sulfhydryl) bands. ( B ) The bar graph represents means ± SEM of the ratio of the 40 kDa Prx6 band to 55 kDa Prx6 band (N = 13 for Alzheimer’s and 5 for control). The symbol * denotes that the value is significantly different from the control value at p < 0.05. ( C ) The scattered graph represents protein carbonylation vs. Prx6 thiol oxidation (N = 18). Pearson correlation coefficient R = 0.723 (positive correlation).
Cm20 Incubation Monitoring System, supplied by Olympus, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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99
Bio-Rad quantification real time pcr detection system
Cysteine oxidation of Prx6 is upregulated in the brains of patients with Alzheimer’s disease. Brain (hippocampus) homogenates from control subjects and patients with Alzheimer’s were investigated for cysteine oxidation of Prx6 using - <t>SulfoBiotics</t> - Protein Redox State Monitoring Kit Plus. A free protein thiol group was labeled with the Protein-SHifter Plus that contains maleimide with a high affinity toward reduced sulfhydryl groups. Each Protein-SHifter causes a 15 kDa shift. After electrophoresis, the Protein-SHifter Plus moiety was eliminated by exposure of the gel to ultraviolet light that increases the efficiency of Western blotting and allows for detection of specific proteins in biological samples. In the case of human Prx6, the protein with fully oxidized cysteine residues migrates at 25 kDa. The protein with one reduced cysteine binds to a Protein-SHifter and migrates at 40 kDa, and the protein with two reduced cysteine residues migrates at 55 kDa. Our previous study determined that the 40 kDa band depicts Prx6, in which the catalytic cysteine (Cys47) is oxidized . ( A ) Representative Western blotting results using the Prx6 antibody showing 25 kDa (0 reduced sulfhydryl), 40 kDa (1 reduced sulfhydryl), and 55 kDa (2 reduced sulfhydryl) bands. ( B ) The bar graph represents means ± SEM of the ratio of the 40 kDa Prx6 band to 55 kDa Prx6 band (N = 13 for Alzheimer’s and 5 for control). The symbol * denotes that the value is significantly different from the control value at p < 0.05. ( C ) The scattered graph represents protein carbonylation vs. Prx6 thiol oxidation (N = 18). Pearson correlation coefficient R = 0.723 (positive correlation).
Quantification Real Time Pcr Detection System, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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96
Bruker Corporation matrix mf ftir
Cysteine oxidation of Prx6 is upregulated in the brains of patients with Alzheimer’s disease. Brain (hippocampus) homogenates from control subjects and patients with Alzheimer’s were investigated for cysteine oxidation of Prx6 using - <t>SulfoBiotics</t> - Protein Redox State Monitoring Kit Plus. A free protein thiol group was labeled with the Protein-SHifter Plus that contains maleimide with a high affinity toward reduced sulfhydryl groups. Each Protein-SHifter causes a 15 kDa shift. After electrophoresis, the Protein-SHifter Plus moiety was eliminated by exposure of the gel to ultraviolet light that increases the efficiency of Western blotting and allows for detection of specific proteins in biological samples. In the case of human Prx6, the protein with fully oxidized cysteine residues migrates at 25 kDa. The protein with one reduced cysteine binds to a Protein-SHifter and migrates at 40 kDa, and the protein with two reduced cysteine residues migrates at 55 kDa. Our previous study determined that the 40 kDa band depicts Prx6, in which the catalytic cysteine (Cys47) is oxidized . ( A ) Representative Western blotting results using the Prx6 antibody showing 25 kDa (0 reduced sulfhydryl), 40 kDa (1 reduced sulfhydryl), and 55 kDa (2 reduced sulfhydryl) bands. ( B ) The bar graph represents means ± SEM of the ratio of the 40 kDa Prx6 band to 55 kDa Prx6 band (N = 13 for Alzheimer’s and 5 for control). The symbol * denotes that the value is significantly different from the control value at p < 0.05. ( C ) The scattered graph represents protein carbonylation vs. Prx6 thiol oxidation (N = 18). Pearson correlation coefficient R = 0.723 (positive correlation).
Matrix Mf Ftir, supplied by Bruker Corporation, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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96
Columbus Instruments whole body oxygen consumption
Cysteine oxidation of Prx6 is upregulated in the brains of patients with Alzheimer’s disease. Brain (hippocampus) homogenates from control subjects and patients with Alzheimer’s were investigated for cysteine oxidation of Prx6 using - <t>SulfoBiotics</t> - Protein Redox State Monitoring Kit Plus. A free protein thiol group was labeled with the Protein-SHifter Plus that contains maleimide with a high affinity toward reduced sulfhydryl groups. Each Protein-SHifter causes a 15 kDa shift. After electrophoresis, the Protein-SHifter Plus moiety was eliminated by exposure of the gel to ultraviolet light that increases the efficiency of Western blotting and allows for detection of specific proteins in biological samples. In the case of human Prx6, the protein with fully oxidized cysteine residues migrates at 25 kDa. The protein with one reduced cysteine binds to a Protein-SHifter and migrates at 40 kDa, and the protein with two reduced cysteine residues migrates at 55 kDa. Our previous study determined that the 40 kDa band depicts Prx6, in which the catalytic cysteine (Cys47) is oxidized . ( A ) Representative Western blotting results using the Prx6 antibody showing 25 kDa (0 reduced sulfhydryl), 40 kDa (1 reduced sulfhydryl), and 55 kDa (2 reduced sulfhydryl) bands. ( B ) The bar graph represents means ± SEM of the ratio of the 40 kDa Prx6 band to 55 kDa Prx6 band (N = 13 for Alzheimer’s and 5 for control). The symbol * denotes that the value is significantly different from the control value at p < 0.05. ( C ) The scattered graph represents protein carbonylation vs. Prx6 thiol oxidation (N = 18). Pearson correlation coefficient R = 0.723 (positive correlation).
Whole Body Oxygen Consumption, supplied by Columbus Instruments, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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99
Fortiori Design LLC moxy monitor
Cysteine oxidation of Prx6 is upregulated in the brains of patients with Alzheimer’s disease. Brain (hippocampus) homogenates from control subjects and patients with Alzheimer’s were investigated for cysteine oxidation of Prx6 using - <t>SulfoBiotics</t> - Protein Redox State Monitoring Kit Plus. A free protein thiol group was labeled with the Protein-SHifter Plus that contains maleimide with a high affinity toward reduced sulfhydryl groups. Each Protein-SHifter causes a 15 kDa shift. After electrophoresis, the Protein-SHifter Plus moiety was eliminated by exposure of the gel to ultraviolet light that increases the efficiency of Western blotting and allows for detection of specific proteins in biological samples. In the case of human Prx6, the protein with fully oxidized cysteine residues migrates at 25 kDa. The protein with one reduced cysteine binds to a Protein-SHifter and migrates at 40 kDa, and the protein with two reduced cysteine residues migrates at 55 kDa. Our previous study determined that the 40 kDa band depicts Prx6, in which the catalytic cysteine (Cys47) is oxidized . ( A ) Representative Western blotting results using the Prx6 antibody showing 25 kDa (0 reduced sulfhydryl), 40 kDa (1 reduced sulfhydryl), and 55 kDa (2 reduced sulfhydryl) bands. ( B ) The bar graph represents means ± SEM of the ratio of the 40 kDa Prx6 band to 55 kDa Prx6 band (N = 13 for Alzheimer’s and 5 for control). The symbol * denotes that the value is significantly different from the control value at p < 0.05. ( C ) The scattered graph represents protein carbonylation vs. Prx6 thiol oxidation (N = 18). Pearson correlation coefficient R = 0.723 (positive correlation).
Moxy Monitor, supplied by Fortiori Design LLC, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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96
TaKaRa human mitochondrial dna mtdna monitoring primer
Cysteine oxidation of Prx6 is upregulated in the brains of patients with Alzheimer’s disease. Brain (hippocampus) homogenates from control subjects and patients with Alzheimer’s were investigated for cysteine oxidation of Prx6 using - <t>SulfoBiotics</t> - Protein Redox State Monitoring Kit Plus. A free protein thiol group was labeled with the Protein-SHifter Plus that contains maleimide with a high affinity toward reduced sulfhydryl groups. Each Protein-SHifter causes a 15 kDa shift. After electrophoresis, the Protein-SHifter Plus moiety was eliminated by exposure of the gel to ultraviolet light that increases the efficiency of Western blotting and allows for detection of specific proteins in biological samples. In the case of human Prx6, the protein with fully oxidized cysteine residues migrates at 25 kDa. The protein with one reduced cysteine binds to a Protein-SHifter and migrates at 40 kDa, and the protein with two reduced cysteine residues migrates at 55 kDa. Our previous study determined that the 40 kDa band depicts Prx6, in which the catalytic cysteine (Cys47) is oxidized . ( A ) Representative Western blotting results using the Prx6 antibody showing 25 kDa (0 reduced sulfhydryl), 40 kDa (1 reduced sulfhydryl), and 55 kDa (2 reduced sulfhydryl) bands. ( B ) The bar graph represents means ± SEM of the ratio of the 40 kDa Prx6 band to 55 kDa Prx6 band (N = 13 for Alzheimer’s and 5 for control). The symbol * denotes that the value is significantly different from the control value at p < 0.05. ( C ) The scattered graph represents protein carbonylation vs. Prx6 thiol oxidation (N = 18). Pearson correlation coefficient R = 0.723 (positive correlation).
Human Mitochondrial Dna Mtdna Monitoring Primer, supplied by TaKaRa, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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96
Columbus Instruments oxymax software
Cysteine oxidation of Prx6 is upregulated in the brains of patients with Alzheimer’s disease. Brain (hippocampus) homogenates from control subjects and patients with Alzheimer’s were investigated for cysteine oxidation of Prx6 using - <t>SulfoBiotics</t> - Protein Redox State Monitoring Kit Plus. A free protein thiol group was labeled with the Protein-SHifter Plus that contains maleimide with a high affinity toward reduced sulfhydryl groups. Each Protein-SHifter causes a 15 kDa shift. After electrophoresis, the Protein-SHifter Plus moiety was eliminated by exposure of the gel to ultraviolet light that increases the efficiency of Western blotting and allows for detection of specific proteins in biological samples. In the case of human Prx6, the protein with fully oxidized cysteine residues migrates at 25 kDa. The protein with one reduced cysteine binds to a Protein-SHifter and migrates at 40 kDa, and the protein with two reduced cysteine residues migrates at 55 kDa. Our previous study determined that the 40 kDa band depicts Prx6, in which the catalytic cysteine (Cys47) is oxidized . ( A ) Representative Western blotting results using the Prx6 antibody showing 25 kDa (0 reduced sulfhydryl), 40 kDa (1 reduced sulfhydryl), and 55 kDa (2 reduced sulfhydryl) bands. ( B ) The bar graph represents means ± SEM of the ratio of the 40 kDa Prx6 band to 55 kDa Prx6 band (N = 13 for Alzheimer’s and 5 for control). The symbol * denotes that the value is significantly different from the control value at p < 0.05. ( C ) The scattered graph represents protein carbonylation vs. Prx6 thiol oxidation (N = 18). Pearson correlation coefficient R = 0.723 (positive correlation).
Oxymax Software, supplied by Columbus Instruments, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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96
tiangen biotech co tgreen monitor blue light instrument
Cysteine oxidation of Prx6 is upregulated in the brains of patients with Alzheimer’s disease. Brain (hippocampus) homogenates from control subjects and patients with Alzheimer’s were investigated for cysteine oxidation of Prx6 using - <t>SulfoBiotics</t> - Protein Redox State Monitoring Kit Plus. A free protein thiol group was labeled with the Protein-SHifter Plus that contains maleimide with a high affinity toward reduced sulfhydryl groups. Each Protein-SHifter causes a 15 kDa shift. After electrophoresis, the Protein-SHifter Plus moiety was eliminated by exposure of the gel to ultraviolet light that increases the efficiency of Western blotting and allows for detection of specific proteins in biological samples. In the case of human Prx6, the protein with fully oxidized cysteine residues migrates at 25 kDa. The protein with one reduced cysteine binds to a Protein-SHifter and migrates at 40 kDa, and the protein with two reduced cysteine residues migrates at 55 kDa. Our previous study determined that the 40 kDa band depicts Prx6, in which the catalytic cysteine (Cys47) is oxidized . ( A ) Representative Western blotting results using the Prx6 antibody showing 25 kDa (0 reduced sulfhydryl), 40 kDa (1 reduced sulfhydryl), and 55 kDa (2 reduced sulfhydryl) bands. ( B ) The bar graph represents means ± SEM of the ratio of the 40 kDa Prx6 band to 55 kDa Prx6 band (N = 13 for Alzheimer’s and 5 for control). The symbol * denotes that the value is significantly different from the control value at p < 0.05. ( C ) The scattered graph represents protein carbonylation vs. Prx6 thiol oxidation (N = 18). Pearson correlation coefficient R = 0.723 (positive correlation).
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Image Search Results


Cysteine oxidation of Prx6 is upregulated in the brains of patients with Alzheimer’s disease. Brain (hippocampus) homogenates from control subjects and patients with Alzheimer’s were investigated for cysteine oxidation of Prx6 using - SulfoBiotics - Protein Redox State Monitoring Kit Plus. A free protein thiol group was labeled with the Protein-SHifter Plus that contains maleimide with a high affinity toward reduced sulfhydryl groups. Each Protein-SHifter causes a 15 kDa shift. After electrophoresis, the Protein-SHifter Plus moiety was eliminated by exposure of the gel to ultraviolet light that increases the efficiency of Western blotting and allows for detection of specific proteins in biological samples. In the case of human Prx6, the protein with fully oxidized cysteine residues migrates at 25 kDa. The protein with one reduced cysteine binds to a Protein-SHifter and migrates at 40 kDa, and the protein with two reduced cysteine residues migrates at 55 kDa. Our previous study determined that the 40 kDa band depicts Prx6, in which the catalytic cysteine (Cys47) is oxidized . ( A ) Representative Western blotting results using the Prx6 antibody showing 25 kDa (0 reduced sulfhydryl), 40 kDa (1 reduced sulfhydryl), and 55 kDa (2 reduced sulfhydryl) bands. ( B ) The bar graph represents means ± SEM of the ratio of the 40 kDa Prx6 band to 55 kDa Prx6 band (N = 13 for Alzheimer’s and 5 for control). The symbol * denotes that the value is significantly different from the control value at p < 0.05. ( C ) The scattered graph represents protein carbonylation vs. Prx6 thiol oxidation (N = 18). Pearson correlation coefficient R = 0.723 (positive correlation).

Journal: International Journal of Molecular Sciences

Article Title: Protein Expression of Angiotensin-Converting Enzyme 2 (ACE2) is Upregulated in Brains with Alzheimer’s Disease

doi: 10.3390/ijms22041687

Figure Lengend Snippet: Cysteine oxidation of Prx6 is upregulated in the brains of patients with Alzheimer’s disease. Brain (hippocampus) homogenates from control subjects and patients with Alzheimer’s were investigated for cysteine oxidation of Prx6 using - SulfoBiotics - Protein Redox State Monitoring Kit Plus. A free protein thiol group was labeled with the Protein-SHifter Plus that contains maleimide with a high affinity toward reduced sulfhydryl groups. Each Protein-SHifter causes a 15 kDa shift. After electrophoresis, the Protein-SHifter Plus moiety was eliminated by exposure of the gel to ultraviolet light that increases the efficiency of Western blotting and allows for detection of specific proteins in biological samples. In the case of human Prx6, the protein with fully oxidized cysteine residues migrates at 25 kDa. The protein with one reduced cysteine binds to a Protein-SHifter and migrates at 40 kDa, and the protein with two reduced cysteine residues migrates at 55 kDa. Our previous study determined that the 40 kDa band depicts Prx6, in which the catalytic cysteine (Cys47) is oxidized . ( A ) Representative Western blotting results using the Prx6 antibody showing 25 kDa (0 reduced sulfhydryl), 40 kDa (1 reduced sulfhydryl), and 55 kDa (2 reduced sulfhydryl) bands. ( B ) The bar graph represents means ± SEM of the ratio of the 40 kDa Prx6 band to 55 kDa Prx6 band (N = 13 for Alzheimer’s and 5 for control). The symbol * denotes that the value is significantly different from the control value at p < 0.05. ( C ) The scattered graph represents protein carbonylation vs. Prx6 thiol oxidation (N = 18). Pearson correlation coefficient R = 0.723 (positive correlation).

Article Snippet: Protein thiol redox states were monitored using the - SulfoBiotics - Protein Redox State Monitoring Kit Plus (Catalog # SB12; Dojindo Molecular Technologies).

Techniques: Control, Labeling, Electrophoresis, Western Blot